Ammina ossidasi (contenente rame)

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ammina ossidasi (contenente rame)
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Numero EC1.4.3.6
ClasseOssidoreduttasi
Nome sistematico
ammina:ossigeno ossidoreduttasi (deaminante) (contenente rame)
Altri nomi
diammina ossidasi; diammino ossidasi; istaminasi; ammina ossidasi; monoammina ossidasi; ammina ossidasi (contenente piridossale); benzilammina ossidasi; istamina deaminasi; istamina ossidasi; Cu-ammina ossidasi; ammina ossigeno ossidoreduttasi; diammina:O2 ossidoreduttasi (deaminante); ammina ossidasi sensibile alla semicarbazide; SSAO
Banche datiBRENDA, EXPASY, GTD, PDB (RCSB PDB PDBe PDBj PDBsum)
Fonte: IUBMB
Modifica dati su Wikidata · Manuale

La ammina ossidasi (contenente rame) è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione:

RCH2NH2 + H2O + O2 ⇄ RCHO + NH3 + H2O2

Si tratta di un gruppo di enzimi in grado di ossidare istamina, monoammine e diammine primarie. Si tratta di chinoproteine contenenti rame. Anche una forma della orotato reduttasi (NADPH) (proveniente da rene di Rattus norvegicus) è in grado di catalizzare la reazione.

La diamminossidasi (DAO) è prodotta dal nostro organismo e si trova principalmente nel duodeno e in misura nettamente minore nel fegato e a livello renale. La diaminossidasi è continuamente prodotta e riversata nel lume intestinale, questo permette ad un organismo sano di eliminare, a livello duodenale, l'istamina contenuta negli alimenti. L'attività dell'enzima DAO è promossa da cofattori, quali vitamina B6, rame, zinco, vitamina C. È inibita da alcool, diversi farmaci, l'alterazione degli enterociti nel tratto gastro-intestinale.

Bibliografia

  • Yamada, H., Adachi, O. and Ogata, K., Amine oxidases of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger, in Agric. Biol. Chem., vol. 29, 1965, pp. 864–869.
  • Yamada, H., Adachi, O. and Ogata, K., Amine oxidases of microorganisms. Part II. Purification and crystallisation of amine oxidase of Aspergillus niger, in Agric. Biol. Chem., vol. 29, 1965, pp. 649–654.
  • Mondovi, B., Costa, M.T., Agro, A.F. and Rotilio, G., Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase, in Arch. Biochem. Biophys., vol. 119, 1967, pp. 373–381, Entrez PubMed 4964016.
  • McEwen, C.M., Jr., Human plasma monoamine oxidase. 1. Purification and identification, in J. Biol. Chem., vol. 240, 1965, pp. 2003–2010, Entrez PubMed 5888801.
  • Haywood, G.W. and Large, P.J., Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source, in Biochem. J., vol. 199, 1981, pp. 187–201, Entrez PubMed 7337701.
  • Buffoni, F. and Blaschko, H., Benzylamine oxidase and histaminase: purification and crystallization of an enzyme from pig plasma, in Proc. R. Soc. Lond. B Biol. Sci., vol. 161, 1964, pp. 153–167, Entrez PubMed 14224405.
  • Blaschko, H., Amine oxidase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (a cura di), The Enzymes, 2nd, New York, Academic Press, 1963, pp. 337–351.
  • Augustinsson, K.-B. and Olsson, B., Esterases in the milk and blood plasma of swine. 1. Substrate specificity and electrophoresis studies, in Biochem. J., vol. 71, 1959, pp. 477–484, Entrez PubMed 13638253.
  • Ameyama, M., Hayashi, M., Matsushita, K., Shinagawa, E. and Adachi, O., Microbial-production of pyrroloquinoline quinone, in Agric. Biol. Chem., vol. 48, 1984, pp. 561–565.
  • Yamada, H., Adachi, O. and Ogata, K., Amine oxidases of microorganisms. Part IV. Further properties of amine oxidase of Aspergillus niger, in Agric. Biol. Chem., vol. 29, 1965, pp. 912–917.
  • Zeller, E.A., Diamine oxidases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (a cura di), The Enzymes, 2nd, New York, Academic Press, 1963, pp. 313–335.
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